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Research Article |
1 Université de
Genève, Centre
Médical Universitaire,
Département de morphologie, 1 Rue Michel
Servet, CH1211 Genève 4, Switzerland
2 Institut de Biologie et de Chimie des
Protéines, UMR5086-CNRS,
Université Lyon I, 7 Passage du Vercors, 69367
Lyon cedex 07, France
3 Laboratoire de Biochimie et Biophysique des
Systèmes
Intégrés,
UMR314 CNRS, CEA, 38054 Grenoble, France
4 Section of Molecular Cell and Developmental Biology and Institute for Cellular
and Molecular Biology, 241 Patterson Bldg., Mail code C0930, University of
Texas, Austin, TX 78712, USA
* Author for correspondence (e-mail: Pierre.Cosson{at}medecine.unige.ch )
Accepted 5 November 2001
Proteins of the Chediak-Higashi/Beige (BEACH) family have been implicated in the function of lysosomes, as well as in signal transduction, but their molecular role is still poorly understood. In Dictyostelium, at least six members of the family can be identified. Here cells with mutations in two of these genes, LVSA and LVSB, were analyzed. Interestingly both mutants exhibited defects in the organization of the endocytic pathway, albeit at distinct stages. In lvsB mutant cells, the regulated secretion of lysosomal enzymes was enhanced, a phenotype reminiscent of the Chediak-Higashi syndrome. LvsA mutant cells exhibited alterations in the organization and function of the early endocytic and phagocytic pathway. The LvsA protein may participate in the signaling pathway, which links adhesion of a particle to the subsequent formation of a phagocytic cup. Further genetic analysis will be necessary to determine whether other members of the BEACH family of proteins are also involved in controlling the organization of the endocytic pathway.
Key words: Beige, BEACH domain, Chediak-Higashi, phagocytosis, lysosome, Lvs, Dictyostelium
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